Proteomics

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Quantitative proteomic profiling of Arabidopsis nuclei reveals accumulation of nucleolar proteins after a prolonged heat stress


ABSTRACT: Heat stress (HS) impacts the nuclear proteome and, subsequently, protein activities in the nucleoplasm and/or different nuclear compartments. In Arabidopsis thaliana, a short exposure to 37°C leads to the loss of the standard tripartite architecture of the nucleolus, the most prominent nuclear substructure, and, consequently, affects the assembly of ribosomes 1. Here, we report a quantitative label-free LC-MS/MS analysis to determine the nuclear proteome of Arabidopsis at 22ºC, HS (37ºC 4 and 24 hours), and a recovery phase. This analysis identified ten distinct groups of proteins based on their protein abundance in the nucleus before, during and after HS: the Early Group (EG), Late Group (LG), Transient Group (TG), Early Persistent Group (EPG), Late Persistent Group (LPG), Burst Group (BG), Early-Like Group (ELG), Late-Like Group (LLG), Transient-Like Group (TLG) and Continuous-Induced Group (CIG). Interestingly, the RNA Pol I subunit NRPA3 and other main nucleolar proteins – such as Nucleolin and Fibrillarin – were detected in the BG and CIG, suggesting that plants require increased nucleolar activity and likely ribosome assembly to restore protein synthesis after HS.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Magali Rompais  

LAB HEAD: Christine CARAPITO

PROVIDER: PXD045038 | Pride | 2024-10-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2018-13-04.mzid.gz Mzid
20181304_SDRF.sdrf.tsv Tabular
F077160.dat Other
F077161.dat Other
F077163.dat Other
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Publications

Proteomic profiling of Arabidopsis nuclei reveals distinct protein accumulation kinetics upon heat stress.

Muñoz-Díaz E E   Fuenzalida-Valdivia I I   Darrière T T   de Bures A A   Blanco-Herrera F F   Rompais M M   Carapito C C   Sáez-Vásquez J J  

Scientific reports 20240814 1


Heat stress (HS) impacts the nuclear proteome and, subsequently, protein activities in different nuclear compartments. In Arabidopsis thaliana, a short exposure to 37 °C leads to loss of the standard tripartite architecture of the nucleolus, the most prominent nuclear substructure, and, consequently, affects the assembly of ribosomes. Here, we report a quantitative label-free LC‒MS/MS (Liquid Chromatography coupled to tandem Mass Spectrometry) analysis to determine the nuclear proteome of Arabid  ...[more]

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